ID A0A1F7ZJJ7_9EURO Unreviewed; 483 AA.
AC A0A1F7ZJJ7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Phosphomevalonate kinase {ECO:0000256|ARBA:ARBA00012958, ECO:0000256|PIRNR:PIRNR017288};
DE EC=2.7.4.2 {ECO:0000256|ARBA:ARBA00012958, ECO:0000256|PIRNR:PIRNR017288};
GN ORFNames=ABOM_011541 {ECO:0000313|EMBL:OGM39622.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM39622.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM39622.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate +
CC ADP; Xref=Rhea:RHEA:16341, ChEBI:CHEBI:30616, ChEBI:CHEBI:57557,
CC ChEBI:CHEBI:58146, ChEBI:CHEBI:456216; EC=2.7.4.2;
CC Evidence={ECO:0000256|ARBA:ARBA00029326};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16342;
CC Evidence={ECO:0000256|ARBA:ARBA00029326};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 2/3. {ECO:0000256|ARBA:ARBA00005017,
CC ECO:0000256|PIRNR:PIRNR017288}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC subfamily. {ECO:0000256|ARBA:ARBA00006495,
CC ECO:0000256|PIRNR:PIRNR017288}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGM39622.1}.
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DR EMBL; LYCR01000189; OGM39622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7ZJJ7; -.
DR STRING; 109264.A0A1F7ZJJ7; -.
DR OrthoDB; 991613at2759; -.
DR UniPathway; UPA00057; UER00099.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004631; F:phosphomevalonate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR InterPro; IPR016005; Erg8.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR035102; Phosphomevalonate_kinase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR31814; -; 1.
DR PANTHER; PTHR31814:SF2; PHOSPHOMEVALONATE KINASE; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF017288; PMK_GHMP_euk; 3.
DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|PIRNR:PIRNR017288, ECO:0000313|EMBL:OGM39622.1};
KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR017288};
KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR017288};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW Steroid biosynthesis {ECO:0000256|PIRNR:PIRNR017288};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221,
KW ECO:0000256|PIRNR:PIRNR017288};
KW Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW Transferase {ECO:0000256|PIRNR:PIRNR017288}.
FT DOMAIN 185..247
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT REGION 54..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 52473 MW; B7B4B0171FC8E760 CRC64;
MSYPPSGSTA LSAPGKVLLT GGYLVLDRNY TGTVIALDAR IHVIVQQLRR GHRRGASSSS
AKGGFDTETL EDGSAVDEKD KEDVVVVRSP QFVNALWEYG IQRCENGGGI KVIQKNEGRA
NPFVETSLNY ALTYISYVAD SKDFGSLSVT ILADTDYYSE TAFSRASESP GRFVNFGVPL
HEAHKTGLGS SAALVTALVS SLVIHRTLQP DDLGPARDKL HNLAQAAHCA AQGKVGSGFD
VAAAIYGSCL YRRFSPSILE SVGDAGSPGF EERLFAVVED VDPKNPWDTE CLDFGLRLPR
GMQMVLCDVE CGSNSPSMVK KVLEWRKQNQ QEADLLWAAL QSNNERLCLQ LKQLAQSPDQ
ESPHDFNDVR NLIQRSRNHL RSMTRKAGVP IEPRVQTELL DAVSAIDGVI GGVVPGAGGY
DAIAVLIHDD PEVLSKLNEL FENWESKVED DFGGKIGTVR LLGVRHGSDG VKNEVLEQYA
GWI
//
